Molecular cloning and primary structure of human 15-lipoxygenase.
Molecular cloning and primary structure of human 15-lipoxygenase.
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DOI：
10.1016/s0006-291x(88)80271-7
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发表时间：
1988-12
影响因子：
3.1
通讯作者：
Elliott Sigal;Charles S. Craik;Ella Highland;D. Grunberger;Lawrence L. Costello;R. A. Dixon;J. A. Nadel
中科院分区：
文献类型：
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作者：
Elliott Sigal;Charles S. Craik;Ella Highland;D. Grunberger;Lawrence L. Costello;R. A. Dixon;J. A. Nadel
从人网织红细胞基因文库中克隆了编码15-脂氧合酶的全长基因。预测的酶一级结构与人5-脂氧合酶和大豆脂氧合酶同工酶I的序列相似性分别为61%和45%。当所有三种脂氧合酶比对时，有两个显著序列同源性的不同区域，包括在所有三种脂氧合酶中保守的五个组氨酸残基的簇。由于组氨酸可以作为具有酶活性的铁的配体，这一区域可能对酶的功能至关重要。这些结果为探索脂肪氧合酶的功能结构域提供了基础。
A full-length cDNA encoding 15-lipoxygenase has been isolated from a human reticulocyte cDNA library. The predicted primary structure of the enzyme exhibits a sequence similarity of 61% and 45% with human 5-lipoxygenase and the soybean lipoxygenase isoenzyme I, respectively. When all three lipoxygneases are aligned, there are two distinct regions of significant sequence identity including a cluster of five histidine residues conserved in all three lipoxygenases. Because histidines can serve as ligands for the enzymatically active iron, this region may be critical to enzymatic function. These results provide a basis for exploring functional domains of lipoxygenases.